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• W4310482512 abstract "ABSTRACT Demixing of proteins and nucleic acids into condensed liquid phases is rapidly emerging as a ubiquitous mechanism underlying the complex spatiotemporal organisation of molecules within the cell. Long disordered regions of low sequence complexity (LCRs) are a common feature of proteins that form liquid-like microscopic biomolecular condensates. In particular, RNA-binding proteins with prion-like composition have been highlighted as key drivers of liquid demixing to form condensates such as the nucleolus, paraspeckles and stress granules. Splicing factor proline- and glutamine-rich (SFPQ) is an RNA- and DNA-binding protein essential for DNA repair and paraspeckle formation. SFPQ contains two LCRs of different length and composition. Here, we show that the shorter C-terminal LCR of SFPQ is the main region responsible for the condensation of SFPQ in vitro and in the cell nucleus. In contrast, we find that, unexpectedly, the longer N-terminal prion-like LCR of SFPQ actually attenuates condensation of the full-length protein, suggesting a more regulatory role in preventing aberrant condensate formation in the cell. Our data add nuance to the emerging understanding of biomolecular condensate formation, by providing the first example of a common multifunctional nucleic acid-binding protein with an extensive prion-like region that serves to regulate rather than drive condensate formation. Abstract Figure" @default.
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• W4310482512 date "2022-11-30" @default.
• W4310482512 modified "2023-09-26" @default.
• W4310482512 title "Different low-complexity regions of SFPQ play distinct roles in the formation of biomolecular condensates" @default.
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• W4310482512 doi "https://doi.org/10.1101/2022.11.30.518278" @default.
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